My research focuses on cellular mechanisms of aggregation of aberrant and damaged proteins. Abnormal polypeptides that escape proteasome-dependent degradation tend to aggregate and can be transported via microtubules to an aggresome, an organelle where aggregated proteins are degraded by autophagy. Protein aggregation plays a major role in various neurodegenerative disorders. We used synphilin 1, a protein implicated in Parkinson disease, as a model to study these processes in cell cultures. We have demonstrated that contrary to popular believes protein aggregation in a cell is not a spontaneous event and relies upon various cellular elements. We found that the cell senses the levels of defective ribosomal products to activate various stress responses including protein aggregation. Furthermore, we demonstrated that mild slowdown of a ribosome can significantly improve the quality of the newly synthesized polypeptides. We found that Bag3-Hsp70 module implicated in carcinogenesis is involved in sensing of the defective ribosomal products and triggering of the stress responses. We work to identify additional elements of this response.